Using an Amino Acid Fluorescence Resonance Energy Transfer Pair To Probe Protein Unfolding: Application to the Villin Headpiece Subdomain and the LysM Domain-Reference-Cited by-同舟云学术

Using an Amino Acid Fluorescence Resonance Energy Transfer Pair To Probe Protein Unfolding: Application to the Villin Headpiece Subdomain and the LysM Domain

Published:2008-09-25 Issue:42 Volume:47 Page:11070-11076
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Glasscock Julie M.¹,Zhu Yongjin¹,Chowdhury Pramit¹,Tang Jia¹,Gai Feng¹

Affiliation:

1. Department of Chemistry and Department of Biochemistry and Molecular Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi8012406

Reference49 articles.

1. Materials for Fluorescence Resonance Energy Transfer Analysis: Beyond Traditional Donor–Acceptor Combinations

2. Probing Protein Folding and Conformational Transitions with Fluorescence

3. Protein folding studied by single-molecule FRET

4. Donor-Donor Energy Migration for Determining Intramolecular Distances in Proteins: I. Application of a Model to the Latent Plasminogen Activator Inhibitor-1 (PAI-1)

5. Conformational Distribution of a 14-Residue Peptide in Solution: A Fluorescence Resonance Energy Transfer Study

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